Pcmt Protein-L-isoaspartate (D-aspartate) O-methyltransferase [Drosophila melanogaster (fruit fly)] - Gene

Summary

Official Symbol: Pcmtprovided by FlyBase
Official Full Name: Protein-L-isoaspartate (D-aspartate) O-methyltransferaseprovided by FlyBase
Primary source: FLYBASE:FBgn0086768
Locus tag: Dmel_CG2152
See related: AllianceGenome:FB:FBgn0086768
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Drosophila melanogaster
Lineage: Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; Drosophilidae; Drosophila; Sophophora
Also known as: CG2152; Dmel\CG2152; dPIMT; pcmt; PCMT; Pimt; PIMT
Summary: Enables protein-L-isoaspartate (D-aspartate) O-methyltransferase activity. Involved in defense response to bacterium. Predicted to be active in cytoplasm. Is expressed in adult head and organism. Orthologous to human PCMT1 (protein-L-isoaspartate (D-aspartate) O-methyltransferase). [provided by Alliance of Genome Resources, Dec 2024]
Orthologs: all
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Genomic context

Location:: 83B1-83B1; 3-47.5 cM

Exon count:: 4

Annotation release	Status	Assembly	Chr	Location
Release 6.54	current	Release 6 plus ISO1 MT (GCF_000001215.4)	3R	NT_033777.3 (5552823..5554316, complement)
Release 5.57	previous assembly	Release 5 (GCF_000001215.2)	3R	NT_033777.2 (1378545..1380038, complement)

Chromosome 3R - NT_033777.3 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Genomic Sequence:

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Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

PIMT was used to monitor the presence of L-isoaspartyl residues in extracellular matrix, type-1 collagen, and fibronectin during aging.
Title: Protein L-isoaspartyl methyltransferase repairs abnormal aspartyl residues accumulated in vivo in type-I collagen and restores cell migration.
A novel structural feature of PIMT is a more open conformation at the C-terminus during its catalytic cycle, thereby allowing the exchange of substrates and products.
Title: Catalytic implications from the Drosophila protein L-isoaspartyl methyltransferase structure and site-directed mutagenesis.

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Pathways from PubChem

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Homology

NCBI Orthologs

Orthologs from OrthoDB

Gene Ontology Provided by FlyBase

Function	Evidence Code	Pubs
enables protein-L-isoaspartate (D-aspartate) O-methyltransferase activity	IBA Inferred from Biological aspect of Ancestor more info
enables protein-L-isoaspartate (D-aspartate) O-methyltransferase activity	IDA Inferred from Direct Assay more info	PubMed
enables protein-L-isoaspartate (D-aspartate) O-methyltransferase activity	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
involved_in defense response to bacterium	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in protein modification process	IEA Inferred from Electronic Annotation more info

Component	Evidence Code	Pubs
is_active_in cytoplasm	IBA Inferred from Biological aspect of Ancestor more info

General protein information

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Preferred Names: Protein-L-isoaspartate (D-aspartate) O-methyltransferase

Names: CG2152-PA; CG2152-PC; Pcmt-PA; Pcmt-PC; protein D-aspartyl, L-isoaspartyl O-methyltransferase; protein isoaspartyl methyltransferase

NP_001262287.1

EC 2.1.1.77

NP_536756.1

EC 2.1.1.77

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

NT_033777.3 Reference assembly

Range

5552823..5554316 complement

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_080508.4 → NP_536756.1 Protein-L-isoaspartate (D-aspartate) O-methyltransferase, isoform A [Drosophila melanogaster]

See identical proteins and their annotated locations for NP_536756.1

Status: REVIEWED

UniProtKB/Swiss-Prot

Q27869, Q9VND1

Related

FBpp0078405

Conserved Domains (2) summary

pfam01135
Location:8 → 221

PCMT; Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT)

cl17173
Location:13 → 223

AdoMet_MTases; S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). ...
NM_001275358.1 → NP_001262287.1 Protein-L-isoaspartate (D-aspartate) O-methyltransferase, isoform C [Drosophila melanogaster]

See identical proteins and their annotated locations for NP_001262287.1

Status: REVIEWED

UniProtKB/TrEMBL

A0A0B4KGK0

Conserved Domains (1) summary

cl17173
Location:13 → 202

AdoMet_MTases; S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). ...